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BERKELEY —People infected with the Human Immunodeficiency Virus (HIV) can stave off the symptoms of AIDS thanks to drug cocktails that mainly target three enzymes produced by the virus, but resistant strains pop up periodically that threaten to thwart these drug combos.

How HIV protein interacts with CD4 receptor

The AIDS virus enters immune cells by binding to CD4 receptors embedded in the membrane (parallel lines) of the cell. But once a virus enters the cell, it makes a protein, Nef, that binds to the protein complex underlying CD4, tagging it for the waste bin. Potential anti-HIV drugs would disable one of the proteins (colored blobs) to which Nef binds, interfering with HIV’s strategy for spreading through the body. Image by James Hurley, UC Berkeley.

Researchers at the University of California, Berkeley, and the National Institutes of Health have instead focused on a fourth protein, Nef, that hijacks host proteins and is essential to HIV’s lethality. The researchers have captured a high-resolution snapshot of Nef bound with a main host protein, and discovered a portion of the host protein that will make a promising target for the next-generation of anti-HIV drugs. By blocking the part of a key host protein to which Nef binds, it may be possible to slow or stop HIV.

“We have imaged the molecular details for the first time,” said structural biologist James H. Hurley, UC Berkeley professor of molecular and cell biology. “Having these details in hand puts us in striking distance of designing drugs to block the binding site and, in doing so, block HIV infectivity.”

Hurley, cell biologist Juan Bonifacino of the Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD) of the National Institutes of Health and their colleagues report their findings in a paper published today (Jan. 28) by the open-access, online journal eLife.